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Mucolipin-3 (Transient receptor potential channel mucolipin 3) (TRPML3)

 MCLN3_HUMAN             Reviewed;         553 AA.
Q8TDD5; Q5T4H5; Q5T4H6; Q9NV09;
19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
01-JUN-2002, sequence version 1.
22-NOV-2017, entry version 125.
RecName: Full=Mucolipin-3;
AltName: Full=Transient receptor potential channel mucolipin 3;
Short=TRPML3;
Name=MCOLN3;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Falardeau J.L., Kennedy J.C., Acierno J.S. Jr., Slaugenhaupt S.A.;
"Cloning of the MCOLN3 gene.";
Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Placenta;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[4]
FUNCTION, ENZYME REGULATION, AND MUTAGENESIS OF HIS-252; HIS-273;
HIS-283 AND ALA-419.
PubMed=18369318; DOI=10.1038/emboj.2008.56;
Kim H.J., Li Q., Tjon-Kon-Sang S., So I., Kiselyov K., Soyombo A.A.,
Muallem S.;
"A novel mode of TRPML3 regulation by extracytosolic pH absent in the
varitint-waddler phenotype.";
EMBO J. 27:1197-1205(2008).
[5]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=19497048; DOI=10.1111/j.1600-0854.2009.00935.x;
Martina J.A., Lelouvier B., Puertollano R.;
"The calcium channel mucolipin-3 is a novel regulator of trafficking
along the endosomal pathway.";
Traffic 10:1143-1156(2009).
[6]
FUNCTION, SUBCELLULAR LOCATION, GLYCOSYLATION, AND MUTAGENESIS OF
ASP-458 AND 458-ASP-ASP-459.
PubMed=19522758; DOI=10.1111/j.1600-0854.2009.00924.x;
Kim H.J., Soyombo A.A., Tjon-Kon-Sang S., So I., Muallem S.;
"The Ca(2+) channel TRPML3 regulates membrane trafficking and
autophagy.";
Traffic 10:1157-1167(2009).
[7]
ENZYME REGULATION, AND MUTAGENESIS OF HIS-283; ALA-419; GLU-449 AND
ASP-459.
PubMed=20378547; DOI=10.1074/jbc.M109.078204;
Kim H.J., Yamaguchi S., Li Q., So I., Muallem S.;
"Properties of the TRPML3 channel pore and its stable expansion by the
Varitint-Waddler-causing mutation.";
J. Biol. Chem. 285:16513-16520(2010).
[8]
SUBUNIT, AND FUNCTION.
PubMed=19885840; DOI=10.1002/jcp.21956;
Curcio-Morelli C., Zhang P., Venugopal B., Charles F.A.,
Browning M.F., Cantiello H.F., Slaugenhaupt S.A.;
"Functional multimerization of mucolipin channel proteins.";
J. Cell. Physiol. 222:328-335(2010).
[9]
FUNCTION.
PubMed=21245134; DOI=10.1074/jbc.M110.169185;
Lelouvier B., Puertollano R.;
"Mucolipin-3 regulates luminal calcium, acidification, and membrane
fusion in the endosomal pathway.";
J. Biol. Chem. 286:9826-9832(2011).
[10]
FUNCTION, AND SUBUNIT.
PubMed=23469151; DOI=10.1371/journal.pone.0058174;
Guo Z., Grimm C., Becker L., Ricci A.J., Heller S.;
"A novel ion channel formed by interaction of TRPML3 with TRPV5.";
PLoS ONE 8:E58174-E58174(2013).
-!- FUNCTION: Nonselective cation channel probably playing a role in
the regulation of membrane trafficking events. Acts as Ca(2+)-
permeable cation channel with inwardly rectifying activity
(PubMed:18369318, PubMed:19497048, PubMed:19522758,
PubMed:19885840). Mediates release of Ca(2+) from endosomes to the
cytoplasm, contributes to endosomal acidification and is involved
in the regulation of membrane trafficking and fusion in the
endosomal pathway (PubMed:21245134). Does not seem to act as
mechanosensory transduction channel in inner ear sensory hair
cells. Proposed to play a critical role at the cochlear
stereocilia ankle-link region during hair-bundle growth (By
similarity). Involved in the regulation of autophagy
(PubMed:19522758). Through association with GABARAPL2 may be
involved in autophagosome formation possibly providing Ca(2+) for
the fusion process (By similarity). Through a possible and
probably tissue-specific heteromerization with MCOLN1 may be at
least in part involved in many lysosome-dependent cellular events
(PubMed:19885840). Possible heteromeric ion channel assemblies
with TRPV5 show pharmacological similarity with TRPML3
(PubMed:23469151). {ECO:0000250|UniProtKB:Q8R4F0,
ECO:0000269|PubMed:18369318, ECO:0000269|PubMed:19497048,
ECO:0000269|PubMed:19522758, ECO:0000269|PubMed:19885840,
ECO:0000269|PubMed:21245134, ECO:0000269|PubMed:23469151,
ECO:0000305}.
-!- ENZYME REGULATION: Inhibited by lumenal H(+) and Na(+)
(PubMed:18369318). The channel pore shows dynamic behavior and
undergoes spontaneous, Ca(2+)-dependent modulation when conducting
Ca(2+) (PubMed:20378547). {ECO:0000269|PubMed:18369318,
ECO:0000269|PubMed:20378547}.
-!- SUBUNIT: Forms homooligomeric complexes; probably tetrameric (By
similarity). Can heterooligomerize with MCOLN1; heteromeric
assemblies have different channel properties as compared to the
respective homooligomers and may be tissue-specific
(PubMed:19885840). May heterooligomerize with TRPV5 to form a
functional distinct ion channel (PubMed:23469151). Interacts with
GABARAPL2 (By similarity). {ECO:0000250|UniProtKB:Q8R4F0,
ECO:0000250|UniProtKB:Q9GZU1, ECO:0000269|PubMed:19885840,
ECO:0000305|PubMed:23469151}.
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
protein {ECO:0000305}. Cell membrane
{ECO:0000269|PubMed:19522758}; Multi-pass membrane protein
{ECO:0000305}. Early endosome membrane
{ECO:0000269|PubMed:19497048, ECO:0000269|PubMed:19522758}; Multi-
pass membrane protein {ECO:0000305}. Late endosome membrane
{ECO:0000269|PubMed:19497048, ECO:0000269|PubMed:19522758}; Multi-
pass membrane protein {ECO:0000305}. Lysosome membrane
{ECO:0000269|PubMed:19522758}; Multi-pass membrane protein
{ECO:0000305}. Cytoplasmic vesicle, autophagosome membrane
{ECO:0000269|PubMed:19522758}. Note=Recycles between the plasma
membrane and intracellular compartments by a dynamin-dependent
endocytic pathway (PubMed:19522758). In the cochlea located at the
base of stereocilia near the position of the ankle links (By
similarity). {ECO:0000250|UniProtKB:Q8R4F0,
ECO:0000269|PubMed:19522758}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q8TDD5-1; Sequence=Displayed;
Name=2;
IsoId=Q8TDD5-2; Sequence=VSP_010823;
-!- DOMAIN: The most N-terminal extracellular/lumenal domain (referred
to as I-II linker or polycystin-mucolipin domain) contributes to a
structure with a four-fold rotational symmetry in a tetrameric
assembly; the structure contains a central highly electronegative
pore with a 14 A diameter. The pore is critical for Ca(2+) and pH
regulation. The protruding structure formed by the I-II linkers
may contain all the interaction sites with lipids and proteins in
the endolysosomal lumen. {ECO:0000250|UniProtKB:Q9GZU1}.
-!- PTM: N-glycosylated. {ECO:0000269|PubMed:19885840}.
-!- SIMILARITY: Belongs to the transient receptor (TC 1.A.4) family.
Polycystin subfamily. MCOLN3 sub-subfamily. {ECO:0000305}.
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EMBL; AF475085; AAL84622.1; -; mRNA.
EMBL; AK001868; BAA91951.1; -; mRNA.
EMBL; AL358789; -; NOT_ANNOTATED_CDS; Genomic_DNA.
CCDS; CCDS58009.1; -. [Q8TDD5-2]
CCDS; CCDS701.1; -. [Q8TDD5-1]
RefSeq; NP_001240622.1; NM_001253693.1. [Q8TDD5-2]
RefSeq; NP_060768.8; NM_018298.10. [Q8TDD5-1]
RefSeq; XP_005271060.1; XM_005271003.1. [Q8TDD5-1]
RefSeq; XP_006710813.1; XM_006710750.1. [Q8TDD5-1]
UniGene; Hs.535239; -.
ProteinModelPortal; Q8TDD5; -.
SMR; Q8TDD5; -.
BioGrid; 120571; 60.
IntAct; Q8TDD5; 1.
STRING; 9606.ENSP00000304843; -.
BindingDB; Q8TDD5; -.
ChEMBL; CHEMBL1293243; -.
GuidetoPHARMACOLOGY; 503; -.
TCDB; 1.A.5.3.4; the polycystin cation channel (pcc) family.
iPTMnet; Q8TDD5; -.
PhosphoSitePlus; Q8TDD5; -.
SwissPalm; Q8TDD5; -.
BioMuta; MCOLN3; -.
DMDM; 50401084; -.
MaxQB; Q8TDD5; -.
PaxDb; Q8TDD5; -.
PeptideAtlas; Q8TDD5; -.
PRIDE; Q8TDD5; -.
Ensembl; ENST00000341115; ENSP00000342698; ENSG00000055732. [Q8TDD5-2]
Ensembl; ENST00000370589; ENSP00000359621; ENSG00000055732. [Q8TDD5-1]
GeneID; 55283; -.
KEGG; hsa:55283; -.
UCSC; uc001dkp.4; human. [Q8TDD5-1]
CTD; 55283; -.
DisGeNET; 55283; -.
EuPathDB; HostDB:ENSG00000055732.12; -.
GeneCards; MCOLN3; -.
HGNC; HGNC:13358; MCOLN3.
HPA; HPA018106; -.
HPA; HPA062137; -.
MIM; 607400; gene.
neXtProt; NX_Q8TDD5; -.
OpenTargets; ENSG00000055732; -.
PharmGKB; PA134947324; -.
eggNOG; KOG3733; Eukaryota.
eggNOG; ENOG410Z1HH; LUCA.
GeneTree; ENSGT00390000017126; -.
HOGENOM; HOG000232158; -.
HOVERGEN; HBG052430; -.
InParanoid; Q8TDD5; -.
KO; K04994; -.
OMA; CGWLILG; -.
OrthoDB; EOG091G026A; -.
PhylomeDB; Q8TDD5; -.
TreeFam; TF317783; -.
Reactome; R-HSA-3295583; TRP channels.
GeneWiki; MCOLN3; -.
GenomeRNAi; 55283; -.
PRO; PR:Q8TDD5; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000055732; -.
CleanEx; HS_MCOLN3; -.
ExpressionAtlas; Q8TDD5; baseline and differential.
Genevisible; Q8TDD5; HS.
GO; GO:0000421; C:autophagosome membrane; IEA:UniProtKB-SubCell.
GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0005262; F:calcium channel activity; TAS:Reactome.
GO; GO:0042491; P:auditory receptor cell differentiation; IEA:Ensembl.
GO; GO:0070588; P:calcium ion transmembrane transport; TAS:Reactome.
GO; GO:0007626; P:locomotory behavior; IEA:Ensembl.
InterPro; IPR013122; PKD1_2_channel.
Pfam; PF08016; PKD_channel; 1.
1: Evidence at protein level;
Alternative splicing; Cell membrane; Complete proteome;
Cytoplasmic vesicle; Disulfide bond; Endosome; Glycoprotein;
Ion channel; Ion transport; Lysosome; Membrane; Reference proteome;
Transmembrane; Transmembrane helix; Transport.
CHAIN 1 553 Mucolipin-3.
/FTId=PRO_0000215367.
TOPO_DOM 1 62 Cytoplasmic. {ECO:0000305}.
TRANSMEM 63 83 Helical. {ECO:0000255}.
TOPO_DOM 84 283 Extracellular. {ECO:0000305}.
TRANSMEM 284 304 Helical. {ECO:0000255}.
TOPO_DOM 305 336 Cytoplasmic. {ECO:0000305}.
TRANSMEM 337 357 Helical. {ECO:0000255}.
TOPO_DOM 358 374 Extracellular. {ECO:0000305}.
TRANSMEM 375 395 Helical. {ECO:0000255}.
TOPO_DOM 396 414 Cytoplasmic. {ECO:0000305}.
TRANSMEM 415 435 Helical. {ECO:0000255}.
TOPO_DOM 436 479 Extracellular. {ECO:0000305}.
TRANSMEM 480 500 Helical. {ECO:0000255}.
TOPO_DOM 501 553 Cytoplasmic. {ECO:0000305}.
REGION 104 118 Extracellular/lumenal pore loop.
{ECO:0000250|UniProtKB:Q9GZU1}.
DISULFID 159 185 {ECO:0000250|UniProtKB:Q9GZU1}.
DISULFID 238 269 {ECO:0000250|UniProtKB:Q9GZU1}.
VAR_SEQ 77 132 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_010823.
MUTAGEN 252 252 H->A: Increases inhibition by lumenal
H(+). Decreases inhibition by lumenal
H(+); when associated with A-283.
{ECO:0000269|PubMed:18369318}.
MUTAGEN 273 273 H->A: Increases inhibition by lumenal
H(+). Decreases inhibition by lumenal
H(+); when associated with A-283.
{ECO:0000269|PubMed:18369318}.
MUTAGEN 283 283 H->A: Constitutive active channel;
abolishes inhibition by lumenal H(+);
retains the Ca(2+)-dependent inactivation
of the Ca(2+) current. Decreases
inhibition by lumenal H(+); when
associated with A-252. Decreases
inhibition by lumenal H(+); when
associated with A-273.
{ECO:0000269|PubMed:18369318}.
MUTAGEN 283 283 H->R: Increases inhibition by lumenal
H(+). {ECO:0000269|PubMed:18369318}.
MUTAGEN 419 419 A->P: Constitutive active channel;
abolishes inhibition by lumenal H(+);
increases the pore diameter.
{ECO:0000269|PubMed:18369318,
ECO:0000269|PubMed:20378547}.
MUTAGEN 449 449 E->A: Constitutive active channel;
greatly impairs inhibition by lumenal
Na(+). {ECO:0000269|PubMed:20378547}.
MUTAGEN 449 449 E->K: Abolishes channel activity.
{ECO:0000269|PubMed:20378547}.
MUTAGEN 458 459 DD->KK: Enhances endocytosis.
{ECO:0000269|PubMed:19522758}.
MUTAGEN 458 458 D->K: Nearly abolishes channel activity;
inhibits starvation-induced autophagy.
{ECO:0000269|PubMed:19522758}.
MUTAGEN 459 459 D->A: Decreases in Ca(2+) permeability
and selectivity; decreases channel pore
dynamic behavior.
{ECO:0000269|PubMed:20378547}.
CONFLICT 9 9 S -> C (in Ref. 2; BAA91951).
{ECO:0000305}.
SEQUENCE 553 AA; 64248 MW; 2E63DA196379F9E3 CRC64;
MADPEVVVSS CSSHEEENRC NFNQQTSPSE ELLLEDQMRR KLKFFFMNPC EKFWARGRKP
WKLAIQILKI AMVTIQLVLF GLSNQMVVAF KEENTIAFKH LFLKGYMDRM DDTYAVYTQS
DVYDQLIFAV NQYLQLYNVS VGNHAYENKG TKQSAMAICQ HFYKRGNIYP GNDTFDIDPE
IETECFFVEP DEPFHIGTPA ENKLNLTLDF HRLLTVELQF KLKAINLQTV RHQELPDCYD
FTLTITFDNK AHSGRIKISL DNDISIRECK DWHVSGSIQK NTHYMMIFDA FVILTCLVSL
ILCIRSVIRG LQLQQEFVNF FLLHYKKEVS VSDQMEFVNG WYIMIIISDI LTIIGSILKM
EIQAKSLTSY DVCSILLGTS TMLVWLGVIR YLGFFAKYNL LILTLQAALP NVIRFCCCAA
MIYLGYCFCG WIVLGPYHDK FRSLNMVSEC LFSLINGDDM FATFAKMQQK SYLVWLFSRI
YLYSFISLFI YMILSLFIAL ITDTYETIKQ YQQDGFPETE LRTFISECKD LPNSGKYRLE
DDPPVSLFCC CKK


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EIAAB44098 Homo sapiens,Human,Long transient receptor potential channel 5,LTrpC5,LTRPC5,LTrpC-5,MLSN1- and TRP-related gene 1 protein,MTR1,Transient receptor potential cation channel subfamily M member 5,TRPM5
EIAAB44093 EREG1,Estrogen-responsive element-associated gene 1 protein,Homo sapiens,Human,KNP3,Long transient receptor potential channel 2,LTrpC2,LTRPC2,LTrpC-2,Transient receptor potential cation channel subfam
18-272-195364 TRPM2 - Rabbit polyclonal to TRPM2; EC 3.6.1.13; Long transient receptor potential channel 2; LTrpC2; LTrpC-2; Transient receptor potential channel 7; TrpC7; Estrogen-responsive element-associated gen 0.05 mg
18-272-195365 TRPM2 - Rabbit polyclonal to TRPM2; EC 3.6.1.13; Long transient receptor potential channel 2; LTrpC2; LTrpC-2; Transient receptor potential channel 7; TrpC7; Estrogen-responsive element-associated gen 0.05 mg
EIAAB44090 Long transient receptor potential channel 1,LTrpC1,Ltrpc1,Melastatin-1,Mouse,Mus musculus,Transient receptor potential cation channel subfamily M member 1,Trpm1
EIAAB44123 Mouse,Mus musculus,Osm-9-like TRP channel 4,OTRPC4,Transient receptor potential cation channel subfamily V member 4,Transient receptor potential protein 12,TRP12,Trp12,TrpV4,Trpv4,Vanilloid receptor-l
EIAAB44097 Calcium-activated non-selective cation channel 1,Long transient receptor potential channel 4,LTrpC4,Ltrpc4,LTrpC-4,Melastatin-like 2,MLS2s,Rat,Rattus norvegicus,Transient receptor potential cation cha
EIAAB44084 Calcium entry channel,Mouse,Mus musculus,Short transient receptor potential channel 6,Transient receptor protein 6,Trp6,TRP-6,TrpC6,Trpc6,Trrp6
EIAAB44125 Osm-9-like TRP channel 4,OTRPC4,Rat,Rattus norvegicus,Transient receptor potential cation channel subfamily V member 4,TrpV4,Trpv4,Vanilloid receptor-related osmotically-activated channel,Vroac,VR-OAC
EIAAB44120 Osm-9-like TRP channel 2,OTRPC2,Rat,Rattus norvegicus,Sac2b,Stretch-activated channel 2B,Transient receptor potential cation channel subfamily V member 2,TrpV2,Trpv2,Vanilloid receptor-like protein 1,
EIAAB44082 Capacitative calcium entry channel 2,CCE2,Mouse,mTRP5,Mus musculus,Short transient receptor potential channel 5,Transient receptor protein 5,Trp5,TRP-5,TrpC5,Trpc5,Trp-related protein 5,Trrp5
EIAAB44075 Mouse,mTrp3,Mus musculus,Receptor-activated cation channel TRP3,Short transient receptor potential channel 3,Transient receptor protein 3,Trp3,TRP-3,TrpC3,Trpc3,Trp-related protein 3,Trrp3


 

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